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Next-Gen Kinase Inhibitors Conference - Day 1 - Cambridge Healthtech Institute



This established and well-recognized kinase conference addresses reoccurring questions about selectivity, safety, resistance and novelty. After many years of research and therapeutic developments of kinase inhibitors, the field still offers new opportunities as novel kinases and their inhibitors are making an appearance. In addition, interest in repurposing of already developed drugs is growing immensely.

“Next-Gen Kinase Inhibitors” addresses what lies ahead, what is in store for the pharmaceutical industry and what new avenues are opening up in regards to technologies and methods used, and in regards to novel targets and therapeutic approaches explored.

Day 1 | Day 2 | Day 3

Monday, June 17

8:00 – 9:00 am Pre-Conference Short Course Registration and Morning Coffee


9:00 – 12:00 pm Short Course: The Art and Science of Kinases* 

Course Instructors:  

Kent D. Stewart, Ph.D., Research Fellow, Structural Biology, AbbVie 

Maricel Torrent, Ph.D., Senior Scientist III, Molecular Modeling, AbbVie


View detailed Short Course agenda 



*Separate Registration Required 


11:00 am Main Conference Registration

1:30 pm Chairperson’s Opening Remarks

Guido Zaman, Ph.D., Founder, Head, Biology, Netherlands Translational Research Center B.V. 


Non-Cancer Indications 

1:40 The Design and Optimization of Selective Protein Kinase C theta (PKCθ) Inhibitors for the Treatment of Autoimmune Diseases

Juan-Miguel Jimenez, Ph.D., Director, Chemistry, Vertex Pharmaceuticals (Europe) Ltd.

Protein kinase C theta (PKCθ) has a central role in T cell activation and survival. Studies in PKCθ-deficient mice have demonstrated that whilst anti-viral responses are PKCθ-independent, T cell responses associated with autoimmune diseases are PKCθ- dependent. Thus, potent and selective inhibition of PKCθ is expected to block autoimmune T cell responses without compromising antiviral immunity. The presentation will describe the design and optimisation of a novel class of potent and selective PKCθ inhibitors, which show exceptional potency in cells and in vivo.

2:10 JAK Inhibition Suppresses Osteoclast Activation through Decreased RANKL Production

Timothy P. LaBranche, DVM, Ph.D., Dipl ACVP, Senior Principal Scientist, Pathologist, Pfizer Drug Safety R&D, Cambridge, MA

Potent inhibition of human T lymphocyte RANKL production by the JAK inhibitor tofacitinib (Xeljanz), combined with the lack of an effect on human osteoclast differentiation/function suggests that JAK inhibition suppresses osteoclast-mediated bone resorption through decreased RANKL production. Although T lymphocytes clearly appear to play a role in osteoclast activation by producing RANKL, it is possible that they do not represent the totality of RANKL production in the arthritic joint.

2:40 Combining Cellular and Biochemical Panel Profiling for the Development of Selective Kinase Inhibitors

Guido Zaman, Ph.D., Founder, Head, Biology, Netherlands Translational Research Center B.V.

Netherlands Translational Research Center B.V. (NTRC) aids in the development of new personalized therapies for the treatment of cancer, autoimmuneand neurodegenerative diseases. Selective kinase inhibitors are optimized for increased target residence time and profiled on large panels of biochemical and cell-based assays. Genotypic, phenotypic and pathway information are combined to determine the optimal compound for a particular patient responder population. Kinase inhibitors are tested in combination with existing drugs to identify new synergies that improve the efficiency of established therapies.

3:10 Refreshment Break in the Exhibit Hall with Poster Viewing

3:40 Effector Kinase Coupling Enables HTS for Inhibitors of HIV-1 Accessory Protein Function

Tom Smithgall, Ph.D., William S. McEllroy Professor of Biochemistry; Chairman, Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine

Nef is an HIV accessory protein that enhances viral infectivity, promotes viral replication, and enables HIV-infected cells to escape host immune surveillance. While an attractive target for antiretroviral drug discovery, Nef presents a challenge for direct HTS assay development because it lacks intrinsic enzymatic or biochemical activity. To circumvent this problem, we developed an HTS-compatible assay that couples Nef to the activation of Hck, a Src-family kinase and Nef effector protein. Using this assay, we screened a large, diverse chemical library and identified small molecules that selectively block Nef-dependentHck activity with low micromolar potency. Of these, a diphenylpyrazolo compound demonstrated sub-micromolar potency in HIV-1 replication assays against a broad range of primary Nef variants. This compound binds directly to the Nefprotein,disrupts Nef dimerization in cells, and blocks Src-family kinase activation downstream as a likely mechanism of action. Coupling of non-enzymatic viral accessory factors to host cell effector proteins amenable to HTS may represent a general strategy for the discovery of new antimicrobial agents.

4:10 Targeting Aurora A Kinase to Overcome CML Acquired Resistance

WenYong Chen, Ph.D., Associate Professor, Department of Cancer Biology, Beckman Research Institute/City of Hope

CML develops acquired resistance to tyrosine kinase inhibitors by acquisition of BCR-ABL kinase domain mutations. We found that an early event for emergence of BCR-ABL mutant cells is mitotic crisis of CML cells triggered by tyrosine kinase inhibitor treatment, and it is controlled by mitotic kinase Aurora A. Specific inhibition of Aurora A is able to prevent acquisition of BCR-ABL mutations and block CML cell relapse from tyrosine kinase inhibitors.

4:40 Q&A with Afternoon Speakers

5:00 Welcome Reception in the Exhibit Hall with Poster Viewing

6:45 Close of Day One



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